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Literature summary extracted from

  • Iyer, S.; La-Borde, P.J.; Payne, K.A.; Parsons, M.R.; Turner, A.J.; Isaac, R.E.; Acharya, K.R.
    Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans A cytosolic enzyme with a di-nuclear active site (2015), FEBS open bio, 5, 292-302 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.9 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3) Caenorhabditis elegans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.9 purified recombinant His-tagged enzyme by sitting drop vapour diffusion method, crystallization buffer containing 17.5% PEG 3350, 0.1 M bis-tris propane, pH 8.5, and 0.2 M sodium malonate is mixed with an equal volume of 3 mg/ml protein in 10 mM Tris/HCl, pH 8.0, and 150 mM NaCl,16°C, X-ray diffraction structure determination and analysis at 1.93 A resolution Caenorhabditis elegans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.9 apstatin 92% inhibition at 0.01 mM, enzyme binding structure modeling, molecular interactions between APP-1 and the ligand, overview. Comparison between Caenorhabditis elegans APP-1-apstatin structure and Escherichia coli APP-1-apstatin structure Caenorhabditis elegans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.9 cytosol
-
 Caenorhabditis elegans 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.9 Zn2+ APP-1 is a dimer that uses dinuclear zinc at the active site Caenorhabditis elegans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.9 143268
-
 analytical ultracentrifugation Caenorhabditis elegans

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.9 Caenorhabditis elegans O44750
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.9 recombinant His-tagged enzyme from Escherichia coli strain BL21 star (DE3) by affinity chromatography and gel filtration Caenorhabditis elegans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.9 bradykinin + H2O i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg Caenorhabditis elegans Arg + des-Arg-bradykinin
-
 ?
3.4.11.9 additional information enzyme APP specifically cleaves the N-terminal Xaa-Pro peptide bond from oligopeptides and is distinct from prolidase, which acts only on dipeptides Caenorhabditis elegans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.9 homodimer 2 * 71977, recombinant His-tagged enzyme without the start Met, mass spectrometry Caenorhabditis elegans
3.4.11.9 More APP-1 is a dimer that uses dinuclear zinc at the active site. The two protomers (MolA and MolB) are held together mainly via hydrophobic interactions. Interfacing residues run along the entire length of the dimer with each subunit contributing 54 residues to the dimer interface Caenorhabditis elegans

Synonyms

EC Number Synonyms Comment Organism
3.4.11.9 aminopeptidase P1
-
 Caenorhabditis elegans
3.4.11.9 APP1
-
 Caenorhabditis elegans
3.4.11.9 X-prolyl aminopeptidase
-
 Caenorhabditis elegans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.9 25
-
 assay at Caenorhabditis elegans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.9 8
-
 assay at Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
3.4.11.9 additional information Caenorhabditis elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases Caenorhabditis elegans
3.4.11.9 physiological function eukaryotic aminopeptidase P1 (APP1) is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are resistant to cleavage by most peptidases, role for APP-1 is in the breakdown of imino-peptides generated during protein catabolism Caenorhabditis elegans